Robert M Clegg
Articles written in Journal of Biosciences
Volume 5 Issue S1 December 1983 pp 105-120
The binding of fluorescently labelled carbohydrates to concanavalin A and wheat germ agglutinin was studied at equilibrium and by the stopped-flow and temperature jump relaxation methods. Ligand were mainly die 4-methylumbelliferyl glycosides of α (1 → 2)-linked manno-oligosaccharides and of β (1 → 4)-linked chito oligosaccharides as limited homologous series. They offer distinct advantages, parti cularly for kinetic studies.
Enthalpie and kinetic considerations suggest that concanavalin A specifically binds a single mannopyranosyl group in α (1 →2)-linked manno-oligosaccharides. This occurs preferentially at the non-reducing end. Glycosylation of a carbohydrate with
Interaction of chito-oligosaccharides with wheat germ agglutinin is complex. With the larger members of the 4-methylumbelliferyl chito-oligosaccharides, binding studies were only possible at low fractional saturation to avoid formation of unsoluble complexes. The binding kinetics of wheat germ agglutinin are faster than with concanavalin A and are consistent with a wheat germ agglutinin binding region composed of two adjacent subsites. For binding of the monoside as well as the bioside, two consistent kinetic models apply. They have common that for each ligand there exist two complexes with comparable population.
Volume 8 Issue 1-2 August 1985 pp 425-436
This contribution illustrates the advantages of some chromophoric and fluorophoric carbohydrate derivatives such as
When monitored by temperature-jump relaxation, binding of MeUmbαGal to the bloodgroup A specific lectin GSAI-A4 from
The complementarity of the peanut agglutinin binding site with Gal
The binding preference of tetravalent
The divalent lectin from